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Dentin sialoprotein (DSP) and phosphophoryn (PP), acidic proteins critical to dentin mineralization, are translated from a single transcript as a DSP-PP precursor that undergoes specific proteolytic processing to generate DSP and PP. The cleavage mechanism continues to be controversial, in part because of the difficulty of obtaining DSP-PP from mammalian cells and dentin matrix. We have infected Sf9 cells with a recombinant baculovirus to produce large amounts of secreted DSP-PP 240 , a variant form of rat DSP-PP. Mass spectrometric analysis shows that DSP-PP 240  secreted by Sf9 cells undergoes specific cleavage at the site predicted from the N-terminal sequence of PP extracted from dentin matrix: SMQG 447 ↓D 448 DPN. DSP-PP 240  is cleaved after secretion by a zinc-dependent activity secreted by Sf9 cells, generating DSP 430  and PP 240  products that are stable in the medium. DSP-PP processing activity is constitutively secreted by Sf9 cells, but secretion is diminished 3 days after infection. Using primers corresponding to the highly conserved catalytic domain of  Drosophila melanogaster  tolloid (a mammalian BMP1 homolog), we isolated a partial cDNA for a  Spodopotera frugiperda  tolloid-related-1 protein (TLR1) that is 78% identical to  Drosophila  TLR1 but only 65% identical to  Drosophila  tolloid.  Tlr1  mRNA decreased rapidly in Sf9 cells after baculovirus infection and was undetectable 4d after infection, paralleling the observed decrease in secretion of the DSP-PP 240  processing activity after infection. Human BMP1 is more similar to Sf9 and  Drosophila  TLR1 than to tolloid, and Sf9 TLR1 is more similar to BMP1 than to other mammalian homologs. Recombinant human BMP1 correctly processed baculovirus-expressed DSP-PP 240  in a dose-dependent manner. Together, these data suggest that the physiologically accurate cleavage of mammalian DSP-PP 240  in the Sf9 cell system represents the action of a conserved processing enzyme and support the proposed role of BMP1 in processing DSP-PP in dentin matrix.

DSP-PP Precursor Protein Cleavage by Tolloid-Related-1 Protein and by Bone Morphogenetic Protein-1